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Food Science and Biotechnology
→ Food Science and Biotechnology 2018 ; 27(1): 57-64
Muscle lysyl oxidase activity and structural/thermal properties of highly cross-linked collagen in jumbo squid (Dosidicus gigas) mantle, fins and arms
Héctor M. Sarabia-Sainz1, Josafat Marina Ezquerra-Brauer1, Hisila C. Santacruz-Ortega2, Ofelia Rouzaud-Sández1, Elisa M. Valenzuela-Soto3, Monica Acosta-Elias4, Wilfrido Torres-Arreola1
1Departamento de Investigación y Posgrado en Alimentos, Universidad de Sonora, Rosales y Blvd. Luis Encinas, P.O. Box 1658, C.P. 83000 Hermosillo, Sonora, Mexico, 2Departamento de Investigación en Polímeros y Materiales, Universidad de Sonora, Rosales y Blvd. Luis Encinas, C.P. 83000 Hermosillo, Sonora, Mexico, 3Centro de Investigación en Alimentación y Desarrollo, A.C. Apdo. Postal 1735, C.P. 83000 Hermosillo, Sonora, Mexico, 4Departamento de Física, Universidad de Sonora, Boulevard Luis Encinas y Rosales s/n, C.P. 83000 Hermosillo, Sonora, Mexico
ABSTRACT
Muscle from mantle, fins and arms of squid (Dosidicus gigas) were compared based on lysyl oxidase activity (LOX), chemical/structural and thermodynamic properties of highly cross-linked collagen. The arms collagen presented the highest temperature (Tp) and enthalpy of transition. The arms collagen thermic properties may be explained by the higher imino amino acid content, proline and lysine hydroxylation degrees. Moreover, among the regions, the collagen from the arms had a more intense β band chain, hydroxymerodesmosine peak in the resonance magnetic nuclear spectra and pyridinoline peak in the Raman spectra. Fins showed the highest LOX activity. The LOX activity was associated with the Tp, proline and lysine hydroxylation degrees. These results implied that the collagen in the arms was more intermolecularly ordered than the mantle and fins, and may provide a theoretical basis for a better understanding of the thermal behaviour of squid tissues during management and processing.
KEYWORD
Chemical structure, Hydroxymerodesmosine, Lysyl oxidase, Squid collagen, Thermal denaturation
Food Science and Biotechnology 2018 ; 27(1): 57-64
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